Q10254 (ALG10_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase
EC=2.4.1.256

Alternative name(s):
Alpha-1,2-glucosyltransferase alg10
Alpha-2-glucosyltransferase alg10
Asparagine-linked glycosylation protein 10
Dolichyl-phosphoglucose-dependent glucosyltransferase alg10

Gene names

Name:	alg10
ORF Names:	SPAC56F8.06c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc2Man9GlcNAc(2)-PP-Dol.
Catalytic activity	Dolichyl beta-D-glucosyl phosphate + D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Glc-alpha-(1->2)-D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the ALG10 glucosyltransferase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	dolichol-linked oligosaccharide biosynthetic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Cellular component	endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: GeneDB_Spombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	dolichyl-phosphate-glucose-glycolipid alpha-glucosyltransferase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 445	445	Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase		PRO_0000215460
Regions
	Transmembrane	7 – 27	21	Helical; Potential
	Transmembrane	54 – 74	21	Helical; Potential
	Transmembrane	81 – 101	21	Helical; Potential
	Transmembrane	123 – 143	21	Helical; Potential
	Transmembrane	170 – 190	21	Helical; Potential
	Transmembrane	192 – 212	21	Helical; Potential
	Transmembrane	218 – 238	21	Helical; Potential
	Transmembrane	256 – 276	21	Helical; Potential
	Transmembrane	298 – 318	21	Helical; Potential
	Transmembrane	336 – 356	21	Helical; Potential
	Transmembrane	364 – 384	21	Helical; Potential
	Transmembrane	408 – 428	21	Helical; Potential
Amino acid modifications
	Glycosylation	76	1	N-linked (GlcNAc...) Potential
	Glycosylation	239	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q10254 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: D031A9914058AE69	FASTA	445	52,279
	10 20 30 40 50 60 MFLGKAIILI LWIFLAFTGL LAIQYYVPNP YLDEIFHIAQ AQRFCRKDWD WDPAITTPPG 70 80 90 100 110 120 LYLVSVALSP FIGCSNVSLR LINWLVGVIG LPWLINDIVS LLNNRKGDVV TYFAYTLSSL 130 140 150 160 170 180 PPLWFFSFLY YTDIGSTFFV LLAYDFALRK SAFSSSVSCF FSLWFRQTNI VWMVFIAVTY 190 200 210 220 230 240 FASNMSFFNP HLAEATFADV LLTIISFLGV FLKNLRRFSC PILSYGAVFC SFLAFLLWNG 250 260 270 280 290 300 SIVLGDKSHH QASIHLSQIN YFLWFFFFFS FPSYIIKYLM SHSRRSKLLS AVFSKKSFLI 310 320 330 340 350 360 VSVLLLIAHF NTIFHPFILA DNRHYLFYVF NRLFRIWWLK YLGPFSYLIL YYFFLDISKL 370 380 390 400 410 420 QMTSLTFFLL ISTTILTLVP APLVEFRYFL LPFLFWRFHL PLPSGRECLM EYALHMVINS 430 440 VTLYIFLFRT FIWPSEPNAL QRFMW

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAA93577.1.
PIR	T38916.
RefSeq	NP_593221.1. NM_001018617.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q10254.
Protein family/group databases
CAZy	GT59. Glycosyltransferase Family 59.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC56F8.06c.1; SPAC56F8.06c.1:pep; SPAC56F8.06c.
GeneID	2543245.
GenomeReviews	Gene locus alg10 in contig CU329670_GR.
KEGG	spo:SPAC56F8.06c.
NMPDR	fig|4896.1.peg.3191.
Organism-specific databases
GeneDB_Spombe	SPAC56F8.06c.
Phylogenomic databases
eggNOG	fuNOG05358.
GeneTree	EFGT00050000003395.
HOGENOM	HBG714502.
OMA	LLTWPYI.
OrthoDB	EOG47WRXP.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000914-MONOMER.
Gene expression databases
ArrayExpress	Q10254.
Family and domain databases
InterPro	IPR016900. Alpha1_2_glucosyltferase_Alg10. IPR007006. Glycosyltransferase_ALG10. [Graphical view]
KO	K03850.
PANTHER	PTHR12989. DIE2_ALG10. 1 hit.
Pfam	PF04922. DIE2_ALG10. 1 hit. [Graphical view]
PIRSF	PIRSF028810. Alpha1_2_glucosyltferase_Alg10. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ALG10_SCHPO

Accession

Primary (citable) accession number: Q10254

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program